Author Archives: Carsten

We are organizing an EMBO Practical Course for studying phase separation in biology!

The course takes place 05 – 13 February 2019 in Dresden at the MPI-CBG, register until 1st Oct. 2018, we are looking forward to seeing you here!   #EMBOphaseseparation / facebook   About the Practical Course The field of cell biology is in the midst of a revolution in the understanding of how cells are […]

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Jie’s paper on the molecular grammar of phase separation is out!

Our latest publication is out now in Cell! Congratulations to Jie and all the co-workers.   In this work, Jie Wang and colleagues worked with a family of prion like proteins (FUS family proteins) and suggest rules that define their phase separation behavior. In cells, FUS family proteins can phase separate into liquid like organelles. However, […]

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Check out our new user’s guide for phase separation assays with purified proteins!

Highlights Membrane-less organelles form by phase separation Membrane-less organelles can be reconstituted from minimal components Phase-separating proteins are difficult to purify and handle We provide guidelines and protocols for working with phase-separating proteins The formation of membrane-less organelles and compartments by protein phase separation is an important way in which cells organize their cytoplasm and […]

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Buffering disease: How the nucleus keeps proteins in check

High RNA concentration maintains RNA-binding proteins in solution and prevents pathological aggregates       Many age-related diseases affect the nervous system. One prominent example of a neurodegenerative disease is Amyotrophic Lateral Sclerosis (ALS). The brain tissue of ALS patients typically shows aggregates of so-called prion-like RNA-binding proteins. In the nucleus, these RNA-binding proteins are […]

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Richard’s review on controlling non-membrane-bound organelles is out

Richard stayed in the lab just about a year but his contributions to the Science of the Hyman lab, not forgetting his many social contributions, have been quite big! Now he wrote a review with Tony for the Philosophical Transactions B on controlling non-membrane-bound organelles. They discuss energetically favourable interactions that could drive condensation, and […]

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Edgar is giving a talk at the CSHL meeting Protein Homeostasis in Health and Disease

The Cold Spring Harbor meeting on Protein Homeostasis is taking place from April 17th-21th and Edgar will speak about how Molecular chaperones control the physical state of membrane-less compartments. Go Edgar!

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Congratulations to Stephanie for her successful collaboration with the Zerial lab!

Rab5 and Alsin regulate stress-activated cytoprotective signaling on mitochondria. Hsu F, Spannl S, Ferguson C, Hyman AA, Parton RG, Zerial M. Elife. 2018 Feb 22;7. pii: e32282. doi: 10.7554/eLife.32282   Mitochondrial stress response is essential for cell survival, and damaged mitochondria are a hallmark of neurodegenerative diseases. Thus, it is fundamental to understand how mitochondria […]

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Congratulations to Sina and Adam for their fellowships!

Sina and Adam received both each an EMBO postdoc fellowship as well as a Marie Curie postdoc fellowship. This is a great success for both of them but as well for the lab. And yes, of course we celebrated it…

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ASAPbio cenference: Transparency, Recognition, and Innovation in Peer Review in the Life Sciences

Tony will be part of the ASAPbio conference on Transparency, Recognition and Innovation in Peer Review in the Life Sciences taking place February 7th to 9th at the HHMI headquarters in Chevy Chase, Maryland. Several aspects of peer review will be discussed in the meeting and importantly, you can follow the conference by live video […]

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Congratulations to Titus and coworkers for his Science paper

Prions are self-propagating protein aggregates that can be transmitted between cells. The aggregates are associated with human diseases. Indeed, pathological prions cause mad cow disease and in humans Creutzfeldt-Jakob disease. The aggregation of prion-like proteins is also associated with neurodegeneration as in ALS. The regions within prion-like proteins that are responsible for their aggregation were […]

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